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1000 results found for “Chitinase”
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Name :
ADA HumanDescription:
Adenosine Deaminase Human Recombinant
Adenosine deaminase, Adenosine aminohydrolase, ADA1, EC 3.5.4.4.
Product # :
ENZ-147Price :
Quantity :
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Shipped with Ice Packs
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Description
ADA Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 383 amino acids (1-363) and having a molecular mass of 42.9 kDa.The ADA is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ADA protein 0.5mg/ml is supplied in 20mM Tris-HCL, pH-8, 1mM DTT and 20% Glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Biological Activity
Specific activity: approximately >25 units/mg. Enzymatic activity was confirmed by measuring the amount of enzyme that deaminates 1.0 umol of adenosine to inosine per minute at pH 7.5 at 25C.More Info
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Introduction
ADA catalyzes the hydrolytic deamination of adenosine and 2-deoxyadenosine. ADA has a vital part in purine metabolism and in adenosine homeostasis. ADA performs as a positive regulator of T-cell coactivation, by binding DPP4 which regulates lymphocyte-epithelial cell adhesion.
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Synonyms
Adenosine deaminase, Adenosine aminohydrolase, ADA1, EC 3.5.4.4.
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Physical Appearance
ADA is supplied as a sterile filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAQTPAFDKP KVELHVHLDG SIKPETILYY GRRRGIALPA NTAEGLLNVI GMDKPLTLPD FLAKFDYYMP AIAGCREAIK RIAYEFVEMK AKEGVVYVEV RYSPHLLANS KVEPIPWNQA EGDLTPDEVV ALVGQGLQEG ERDFGVKARS ILCCMRHQPN WSPKVVELCK KYQQQTVVAI DLAGDETIPG SSLLPGHVQA YQEAVKSGIH RTVHAGEVGS AEVVKEAVDI LKTERLGHGY HTLEDQALYN RLRQENMHFE ICPWSSYLTG AWKPDTEHAV IRLKNDQANY SLNTDDPLIF KSTLDTDYQM TKRDMGFTEE EFKRLNINAA KSSFLPEDEK RELLDLLYKA YGMPPSASAG QNL
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
MMP9 Human, Sf9Description:
Matrix Metalloproteinase-9 Human Recombinant, Sf9
Matrix metalloproteinase-9, MMP-9, 92 kDa gelatinase, Gelatinase B, GELB, MMP9, CLG4B.
Product # :
ENZ-1091Price :
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Description
MMP9 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 694 amino acids (20-707a.a.) and having a molecular mass of 77.1 kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). MMP9 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
MMP9 protein solution ( 0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
MMP9 is part of the matrix metalloproteinase family. MMP enzymes take part in the dismantle of extracellular matrix in different physiological pathways, for instance wound healing, bone development, reproduction etc. the enzyme is also involved in pathological pathways: metastasis, arthritis and intracerebral hemorrhage.
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Synonyms
Matrix metalloproteinase-9, MMP-9, 92 kDa gelatinase, Gelatinase B, GELB, MMP9, CLG4B.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
APRQRQSTLV LFPGDLRTNL TDRQLAEEYL YRYGYTRVAE MRGESKSLGP ALLLLQKQLS LPETGELDSA TLKAMRTPRC GVPDLGRFQTFEGDLKWHHH NITYWIQNYS EDLPRAVIDD AFARAFALWS AVTPLTFTRV YSRDADIVIQ FGVAEHGDGY PFDGKDGLLA HAFPPGPGIQ GDAHFDDDEL WSLGKGVVVP TRFGNADGAA CHFPFIFEGR SYSACTTDGR SDGLPWCSTT ANYDTDDRFG FCPSERLYTQ DGNADGKPCQ FPFIFQGQSY SACTTDGRSD GYRWCATTAN YDRDKLFGFC PTRADSTVMG GNSAGELCVF PFTFLGKEYS TCTSEGRGDG RLWCATTSNF DSDKKWGFCP DQGYSLFLVA AHEFGHALGL DHSSVPEALM YPMYRFTEGP PLHKDDVNGI RHLYGPRPEP EPRPPTTTTP QPTAPPTVCP TGPPTVHPSE RPTAGPTGPP SAGPTGPPTA GPSTATTVPL SPVDDACNVN IFDAIAEIGN QLYLFKDGKY WRFSEGRGSR PQGPFLIADK WPALPRKLDS VFEERLSKKL FFFSGRQVWV YTGASVLGPR RLDKLGLGAD VAQVTGALRS GRGKMLLFSG RRLWRFDVKA QMVDPRSASE VDRMFPGVPL DTHDVFQYRE KAYFCQDRFY WRVSSRSELN QVDQVGYVTY DILQCPEDHH HHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
DECR1 HumanDescription:
2,4-Dienoyl CoA Reductase 1 Human Recombinant
2,4-dienoyl-CoA reductase, mitochondrial, 2,4-dienoyl-CoA reductase [NADPH], 4-enoyl-CoA reductase [NADPH], DECR1, DECR, NADPH, SDR18C1.
Product # :
ENZ-102Price :
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Description
DECR1 Human Recombinant fused to 21 amino acid His Tag at N-terminal produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 322 amino acids (35-335 a.a.) and having a molecular mass of 34.4kDa. The DECR1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The DECR1 solution contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
DECR1 is a mitochondrial protein which exists as a homotetramer and is a member of a family of short-chain dehydrogenases/reductases. DECR1 acts as an auxiliary enzyme of beta-oxidation andt partakes in the metabolism of unsaturated fatty enoyl-CoA esters. in particular, DECR1 uses NADP+ to catalyze the reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA that can subsequently be used as an intermediate in the Krebs cycle. Furthermore, DECR1 is believed to work as a tumor suppressor, possibly downregulating the expression of Neu and slowing the rate of tumorigenesis.
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Synonyms
2,4-dienoyl-CoA reductase, mitochondrial, 2,4-dienoyl-CoA reductase [NADPH], 4-enoyl-CoA reductase [NADPH], DECR1, DECR, NADPH, SDR18C1.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MNTEALQSKF FSPLQKAMLP PNSFQGKVAF ITGGGTGLGK GMTTLLSSLG AQCVIASRKM DVLKATAEQI SSQTGNKVHA IQCDVRDPDM VQNTVSELIK VAGHPNIVIN NAAGNFISPT ERLSPNAWKT ITDIVLNGTA FVTLEIGKQL IKAQKGAAFL SITTIYAETG SGFVVPSASA KAGVEAMSKS LAAEWGKYGM RFNVIQPGPI KTKGAFSRLD PTGTFEKEMI GRIPCGRLGT VEELANLAAF LCSDYASWIN GAVIKFDGGE EVLISGEFND LRKVTKEQWD TIEELIRKTK GS.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
HMGCL Human, Sf9Description:
3-Hydroxymethyl-3-Methylglutaryl-CoA Lyase Human Recombinant, Sf9
3-Hydroxymethyl-3-Methylglutaryl-CoA Lyase, 3-Hydroxymethyl-3-Methylglutaryl-Coenzyme A Lyase, 3-Hydroxy-3-Methylglutarate-CoA Lyase, Hydroxymethylglutaricaciduria, HMG-CoA Lyase, EC 4.1.3.4, HL, Mitochondrial 3-Hydroxy-3-Methylglutaryl-CoA Lyase, Hydroxymethylglutaryl-CoA Lyase, Mitochondrial, 3-Hydroxy-3-Methylglutaryl-CoA Lyase, Hydroxymethylglutaryl-CoA lyase, mitochondrial, HMG-CoA lyase, 3-hydroxy-3-methylglutarate-CoA lyase.
Product # :
ENZ-1056Price :
Quantity :
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Description
HMGCL Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 305 amino acids (28-325 a.a.) and having a molecular mass of 32.5kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). HMGCL is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
HMGCL protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4), 20% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Hydroxymethylglutaryl-CoA lyase (HMGCL) is a mitochondrial matrix protein which is a member of the HMG-CoA lyase family. HMGCL is a homodimer and participates in leucine catabolism and ketogenesis, the hepatic synthesis of ketone bodies which, during fasting, provides a major source of energy for the heart, brain and kidney. More precisely, HMGCL catalyzes the final step of these processes, the cleavage of 3-hydroxy-3-methylglutaryl-CoA to acetoacetic acid and acetyl-CoA.
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Synonyms
3-Hydroxymethyl-3-Methylglutaryl-CoA Lyase, 3-Hydroxymethyl-3-Methylglutaryl-Coenzyme A Lyase, 3-Hydroxy-3-Methylglutarate-CoA Lyase, Hydroxymethylglutaricaciduria, HMG-CoA Lyase, EC 4.1.3.4, HL, Mitochondrial 3-Hydroxy-3-Methylglutaryl-CoA Lyase, Hydroxymethylglutaryl-CoA Lyase, Mitochondrial, 3-Hydroxy-3-Methylglutaryl-CoA Lyase, Hydroxymethylglutaryl-CoA lyase, mitochondrial, HMG-CoA lyase, 3-hydroxy-3-methylglutarate-CoA lyase.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MTLPKRVKIV EVGPRDGLQN EKNIVSTPVK IKLIDMLSEA GLSVIETTSF VSPKWVPQMG DHTEVLKGIQ KFPGINYPVL TPNLKGFEAA VAAGAKEVVI FGAASELFTK KNINCSIEES FQRFDAILKA AQSANISVRG YVSCALGCPY EGKISPAKVA EVTKKFYSMG CYEISLGDTI GVGTPGIMKD MLSAVMQEVP LAALAVHCHD TYGQALANTL MALQMGVSVV DSSVAGLGGC PYAQGASGNL ATEDLVYMLE GLGIHTGVNL QKLLEAGNFI CQALNRKTSS KVAQATCKLH HHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
SPR HumanDescription:
Sepiapterin Reductase Human Recombinant
SDR38C1, SPR, Dystonia, Sepiapterin reductase.
Product # :
ENZ-411Price :
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Description
Sepiapterin Reductase produced in E.Coli is a single,non-glycosylated polypeptide chain containing 281 amino acids (1-261 a.a.) and having a molecular mass of 30.2 kDa.Sepiapterin Reductase is expressed with a 20 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SPR solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Sepiapterin Reductase is an aldo-keto reductase that catalyzes the NADPH-dependent reduction of pteridine derivatives and is essential in the biosynthesis of BH4. Mutations in Sepiapterin Reductase gene result in DOPA-responsive dystonia due to sepiaterin reductase deficiency defined by the presence of sustained involuntary muscle contractions, often leading to abnormal postures. Sepiapterin reductase is part of the short-chain dehydrogenase/reductase family which reduces exogenous carbonyl compounds as well as phenylpropanedione. Sepiapterin reductase is an important enzyme for the biosynthesis of tetrahydrobiopterin, an necessary cofactor for aromatic amino acid hydrolases together with tyrosine hydroxylase, the rate-limiting enzyme in DOPA synthesis.
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Synonyms
SDR38C1, SPR, Dystonia, Sepiapterin reductase.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MEGGLGRAVC LLTGASRGFG RTLAPLLASL LSPGSVLVLS ARNDEALRQL EAELGAERSG LRVVRVPADL GAEAGLQQLL GALRELPRPK GLQRLLLINN AGSLGDVSKG FVDLSDSTQV NNYWALNLTS MLCLTSSVLK AFPDSPGLNR TVVNISSLCA LQPFKGWALY CAGKAARDML FQVLALEEPN VRVLNYAPGP LDTDMQQLAR ETSVDPDMRK GLQELKAKGK LVDCKVSAQK LLSLLEKDEF KSGAHVDFYD K.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
ACAA1 HumanDescription:
Acetyl-COA Acyltransferase Human Recombinant
ACAA, PTHIO, THIO.
Product # :
ENZ-251Price :
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Description
ACAA1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 419 amino acids (27-424 a.a.) and having a molecular mass of 43.8 kDa. The ACAA1 is fused to 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ACAA1 1mg/ml protein solution contains 20mM Tris pH-8, 0.1M NaCl, 1mM DTT & 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
ACAA1 is part of the thiolase family of enzymes and is takes part in lipid metabolism. ACAA1 enzyme is localized to the peroxisome and catalyzes the conversion of acyl-CoA and acetyl-CoA to 3-oxoacyl-CoA in the fatty acid oxidation pathway. ACAA1 shows high enzymatic activity in liver, kidney, intestine and white adipose tissue in rats. ACAA1 deficiency causes pseudo-Zellweger syndrome.
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Synonyms
ACAA, PTHIO, THIO.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
ACAA1 Human although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MLSGAPQASA ADVVVVHGRR TAICRAGRGG FKDTTPDELL SAVMTAVLKD VNLRPEQLGD ICVGNVLQPG AGAIMARIAQ FLSDIPETVP LSTVNRQCSS GLQAVASIAG GIRNGSYDIG MACGVESMSL ADRGNPGNIT SRLMEKEKAR DCLIPMGITS ENVAERFGIS REKQDTFALA SQQKAARAQS KGCFQAEIVP VTTTVHDDKG TKRSITVTQD EGIRPSTTME GLAKLKPAFK KDGSTTAGNS SQVSDGAAAI LLARRSKAEE LGLPILGVLR SYAVVGVPPD IMGIGPAYAI PVALQKAGLT VSDVDIFEIN EAFASQAAYC VEKLRLPPEK VNPLGGAVAL GHPLGCTGAR QVITLLNELK RRGKRAYGVV SMCIGTGMGA AAVFEYPGN.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
ADSL HumanDescription:
Adenylosuccinate Lyase Human Recombinant
Adenylosuccinate lyase, ASL, Adenylosuccinase, ASase, ADSL, AMPS.
Product # :
ENZ-188Price :
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Description
ADSL Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 520 amino acids (1-484) and having a molecular mass of 59kDa.ADSL is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ADSL solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 40% glycerol and 0.1M NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Adenylosuccinate lyase (ADSL) is an enzyme which converts adenylosuccinate to AMP and fumarate as part of the purine nucleotide cycle. ADSL is involved in both de novo synthesis of purines and formation of adenosine monophosphate from inosine monophosphate. ADSL catalyzes 2 reactions in AMP biosynthesis: the removal of a fumarate from succinylaminoimidazole carboxamide (SAICA) ribotide to yield aminoimidazole carboxamide ribotide (AICA) and removal of fumarate from adenylosuccinate to yield AMP. Defects in the ADSL are the cause of adenylosuccinase deficiency (ADSL deficiency). ADSL deficiency is an autosomal recessive disorder distinguished by the accumulation in the body fluids of succinylaminoimidazole-carboxamide riboside (SAICA-riboside) and succinyladenosine (S-Ado). Adenylosuccinase deficiency results in succinylpurinemic autism, psychomotor retardation, and in some cases, growth retardation associated with muscle wasting and epilepsy.
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Synonyms
Adenylosuccinate lyase, ASL, Adenylosuccinase, ASase, ADSL, AMPS.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMAAG GDHGSPDSYR SPLASRYASP EMCFVFSDRY KFRTWRQLWL WLAEAEQTLG LPITDEQIQE MKSNLENIDF KMAAEEEKRL RHDVMAHVHT FGHCCPKAAG IIHLGATSCY VGDNTDLIIL RNALDLLLPK LARVISRLAD FAKERASLPT LGFTHFQPAQ LTTVGKRCCL WIQDLCMDLQ NLKRVRDDLR FRGVKGTTGT QASFLQLFEG DDHKVEQLDK MVTEKAGFKR AFIITGQTYT RKVDIEVLSV LASLGASVHK ICTDIRLLAN LKEMEEPFEK QQIGSSAMPY KRNPMRSERC CSLARHLMTL VMDPLQTASV QWFERTLDDS ANRRICLAEA FLTADTILNT LQNISEGLVV YPKVIERRIR QELPFMATEN IIMAMVKAGG SRQDCHEKIR VLSQQAASVV KQEGGDNDLI ERIQVDAYFS PIHSQLDHLL DPSSFTGRAS QQVQRFLEEE VYPLLKPYES VMKVKAELCL.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
AKR1B1 HumanDescription:
Aldose Reductase Human Recombinant
Aldehyde Reductase, EC 1.1.1.21, ALR2, ALDR1, MGC1804, Aldo-keto reductase family1 member B1, Aldose Reductase, AKR1B1, AR, ADR.
Product # :
ENZ-390Price :
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Description
AKR1B1 Human Recombinant amino produced in E.Coli is a single, non-glycosylated polypeptide chain containing 316 amino acids having a molecular mass of 35.8 kDa.The AKR1B1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The 1mg/ml protein solution contains 20mM Tris-HCl buffer pH 8, 10% glycerol, and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 800pmol/min/ug, and is defined as the amount of enzyme that catalyze the reduction of 1.0 pmole DL-glyceraldehyde in the presence of NADPH per minute at pH7.0 at 37°C.More Info
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Introduction
AKR1B1 is part of the aldo/keto reductase superfamily, which consists of more than 40 known enzymes and proteins. AKR1B1 catalyzes the reduction several aldehydes, including the aldehyde form of glucose, and thus involved in the development of diabetic complications by catalyzing the reduction of glucose to sorbitol. AKR1B1 catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols. Transgenic mice over expressing human aldose reductase show that AKR1B1 is a key player in ischemic injury and impairment of functional and metabolic recovery after ischemia. Aldose Reductase is an obligatory mediator of TNF-alpha signaling leading to an increase in the expression of adhesion molecules and increased binding of monocytes to the endothelium. AKR1B1 is a critical regulator of TNF-alpha-induced apoptotic signaling in endothelial cells.
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Synonyms
Aldehyde Reductase, EC 1.1.1.21, ALR2, ALDR1, MGC1804, Aldo-keto reductase family1 member B1, Aldose Reductase, AKR1B1, AR, ADR.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MASRLLLNNG AKMPILGLGT WKSPPGQVTE AVKVAIDVGY RHIDCAHVYQ NENEVGVAIQ EKLREQVVKR EELFIVSKLW CTYHEKGLVK GACQKTLSDL KLDYLDLYLI HWPTGFKPGK EFFPLDESGN VVPSDTNILD TWAAMEELVD EGLVKAIGIS NFNHLQVEMI LNKPGLKYKP AVNQIECHPY LTQEKLIQYC QSKGIVVTAY SPLGSPDRPW AKPEDPSLLE DPRIKAIAAK HNKTTAQVLI RFPMQRNLVV IPKSVTPERI AENFKVFDFE LSSQDMTTLL SYNRNWRVCA LLSCTSHKDY PFHEEF.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
DDT HumanDescription:
D-Dopachrome Tautomerase Human Recombinant
EC 4.1.1.84, DDCT, D-dopachtome decarboxylase, D-Dopachrome Tautomerase.
Product # :
ENZ-527Price :
Quantity :
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Description
DDT Recombinant E.coli produced in E.Coli is a single, non-glycosylated polypeptide chain containing 138 amino acids (1-118 a.a.) and having a molecular mass of 14.8 kDa. The DDT is fused to a 20 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
DDT Human solution containing 20mM Tris-HCl pH-8, & 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
DDT is an enzyme that catayzes the tautomerization of D-dopachrome to give 5,6-dihydroxyindole (DHI). DDT is part of the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. DDT shares a homologous amino acid sequence (33% identical) with MIF and has similar tautomerase activity. DDT functions a proinflammatory cytokine.
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Synonyms
EC 4.1.1.84, DDCT, D-dopachtome decarboxylase, D-Dopachrome Tautomerase.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MPFLELDTNL PANRVPAGLE KRLCAAAASI LGKPADRVNV TVRPGLAMAL SGSTEPCAQL SISSIGVVGT AEDNRSHSAH FFEFLTKELA LGQDRILIRF FPLESWQIGK IGTVMTFL.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
PGAM2 HumanDescription:
Phosphoglycerate Mutase 2 Human Recombinant
Phosphoglycerate mutase 2, BPG-dependent PGAM 2, Muscle-specific phosphoglycerate mutase, Phosphoglycerate mutase isozyme M, PGAM-M, PGAM2, PGAMM, GSD10.
Product # :
ENZ-578Price :
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Shipped with Ice Packs
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Description
PGAM2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 273 amino acids (1-253) and having a molecular mass of 30.9kDa.PGAM2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PGAM2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Phosphoglycerate mutase 2 (PGAM2) is a member of the phosphoglycerate mutase family. PGAM is a dimeric enzyme which contains in separate tissues, different proportions of a slow-migrating muscle (MM) isozyme, a fast-migrating brain (BB) isozyme, and a hybrid form (MB). PGAM (Phosphoglycerate mutase) catalyzes the reversible reaction of 3-phosphoglycerate (3-PGA) to 2-phosphoglycerate (2-PGA) in the glycolytic pathway. PGAM2 gene mutations cause muscle phosphoglycerate mutase efficiency, otherwise known as glycogen storage disease X.
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Synonyms
Phosphoglycerate mutase 2, BPG-dependent PGAM 2, Muscle-specific phosphoglycerate mutase, Phosphoglycerate mutase isozyme M, PGAM-M, PGAM2, PGAMM, GSD10.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MATHRLVMVR HGESTWNQEN RFCGWFDAEL SEKGTEEAKR GAKAIKDAKM EFDICYTSVL KRAIRTLWAI LDGTDQMWLP VVRTWRLNER HYGGLTGLNK AETAAKHGEE QVKIWRRSFD IPPPPMDEKH PYYNSISKER RYAGLKPGEL PTCESLKDTI ARALPFWNEE IVPQIKAGKR VLIAAHGNSL RGIVKHLEGM SDQAIMELNL PTGIPIVYEL NKELKPTKPM QFLGDEETVR KAMEAVAAQG KAK.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
GALNT1 HumanDescription:
Polypeptide N-Acetylgalactosaminyltransferase 1 Human Recombinant
Polypeptide N-acetylgalactosaminyltransferase 1, GALNT1, GALNAC-T1
Product # :
enz-1098Price :
Quantity :
Shipping Method :
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Description
GALNT1 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 528 amino acids (41-559a.a.) and having a molecular mass of 60.4kDa.GALNT1 is expressed with an 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
GALNT1 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) containing 0.1M NaCl and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
The specific activity which is defined as the amount of enzyme that transfer 1.0 pmole of GalNAc from UDP-GalNAc to peptide EA2 per minute at pH 8.0 at 37C is > 300 pmol/min/ug.
More Info
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Introduction
Polypeptide N-Acetylgalactosaminyltransferase 1 (Galnt1) is a part of the UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes. The initial reaction in O-linked oligosaccharide biosynthesis is catalyzed by Glant1, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Moreover, Galnt1 is implicated in the glycosylation of proteins vital for bone formation for instance osteopontin and bone sialoprotein.
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Synonyms
Polypeptide N-acetylgalactosaminyltransferase 1, GALNT1, GALNAC-T1
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Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
ADPGLPAGDV LEPVQKPHEG PGEMGKPVVI PKEDQEKMKE MFKINQFNLM ASEMIALNRS
LPDVRLEGCK TKVYPDNLPT TSVVIVFHNE AWSTLLRTVH SVINRSPRHM IEEIVLVDDA
SERDFLKRPL ESYVKKLKVP VHVIRMEQRS GLIRARLKGA AVSKGQVITF LDAHCECTVG
WLEPLLARIK HDRRTVVCPI IDVISDDTFE YMAGSDMTYG GFNWKLNFRW YPVPQREMDR
RKGDRTLPVR TPTMAGGLFS IDRDYFQEIG TYDAGMDIWG GENLEISFRI WQCGGTLEIV
TCSHVGHVFR KATPYTFPGG TGQIINKNNR RLAEVWMDEF KNFFYIISPG VTKVDYGDIS
SRVGLRHKLQ CKPFSWYLEN IYPDSQIPRH YFSLGEIRNV ETNQCLDNMA RKENEKVGIF
NCHGMGGNQV FSYTANKEIR TDDLCLDVSK LNGPVTMLKC HHLKGNQLWE YDPVKLTLQH
VNSNQCLDKA TEEDSQVPSI RDCNGSRSQQ WLLRNVTLPE IFHHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
GOT2 MouseDescription:
Glutamic-Oxaloacetic Transaminase 2 Mouse Recombinant
Transaminase A, KAT4, KATIV, KAT-4, KAT-IV,Kynurenine Aminotransferase 4.
Product # :
ENZ-1095Price :
Quantity :
Shipping Method :
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Description
GOT2 Recombinant Mouse produced in E.Coli is a single, non-glycosylated polypeptide chain containing 424 amino acids (30-430 a.a.) and having a molecular mass of 46.8kDa. Mouse GOT2 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GOT2 solution (0.5mg/ml) contains PBS, pH 7.4 and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Activity is greater than 20 units/mg, and is defined as the amount of enzyme that converts 1umole of alpha-ketoglutarate to L-Glutamate per minute at pH 8.0 at 25℃.
More Info
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Introduction
GOT2 is a pyridoxal phosphate-dependent enzyme which is found in cytoplasmic and inner-membrane mitochondrial forms, GOT1 and GOT2. GOT2 takes part in amino acid metabolism and the urea and tricarboxylic acid cycles. Both enzymes are homodimeric and demonstrate close homology.
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Synonyms
Transaminase A, KAT4, KATIV, KAT-4, KAT-IV,Kynurenine Aminotransferase 4.
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Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSSWWTHVEM GPPDPILGVT EAFKRDTNSK KMNLGVGAYR DDNGKPYVLP SVRKAEAQIA AKNLDKEYLP IGGLAEFCKA SAELALGENN EVLKSGRFVT VQTISGTGAL RVGASFLQRF FKFSRDVFLP KPSWGNHTPI FRDAGMQLQG YRYYDPKTCG FDFSGALEDI SKIPEQSVLL LHACAHNPTG VDPRPEQWKE IASVVKKKNL FAFFDMAYQG FASGDGDKDA WAVRHFIEQG INVCLCQSYA KNMGLYGERV GAFTVVCKDA EEAKRVESQL KILIRPLYSN PPLNGARIAA TILTSPDLRK QWLQEVKGMA DRIISMRTQL VSNLKKEGSS HNWQHITDQI GMFCFTGLKP EQVERLTKEF SVYMTKDGRI SVAGVTSGNV GYLAHAIHQV.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
NAT6 HumanDescription:
N-Acetyltransferase 6 Human Recombinant
Protein fusion-2, FUS2, FUS-2, NAT6, N-acetyltransferase 6, Protein fus-2.
Product # :
ENZ-410Price :
Quantity :
Shipping Method :
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Description
Recombinant Human NAT6 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 328 amino acids (1-308 a.a.) and having a molecular mass of 35.9 kDa. NAT6 is fused to a 20 amino acid His Tag at N-terminus and purified by conventional chromatography techniques.
Source
Escherichia Coli.
Formulation
The NAT6 protein solution contains 20mM Tris-HCl, pH-8, 100mM NaCl and 20% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
NAT6 is an enzyme that catalyzes the transfer of acetyl groups from acetyl-CoA to acrylamines. NAT6 is located mainly in the cytoplasm and its activity has been recognized by its feasibility to acetylate the N-terminus of proteins using a ping-pong-like mechanism and by its substrate specificity. Given that the NAT6 gene maps to the chromosomal region 3p21.3, which includes at least one tumor suppressor gene, the function of NAT6 plays an important role in cancer.
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Synonyms
Protein fusion-2, FUS2, FUS-2, NAT6, N-acetyltransferase 6, Protein fus-2.
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Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MQELTLSPGP AKLTPTLDPT HRMELILSTS PAELTLDPAC QPKLPLDSTC QPEMTFNPGP TELTLDPEHQ PEETPAPSLA ELTLEPVHRR PELLDACADL INDQWPRSRT SRLHSLGQSS DAFPLCLMLL SPHPTLEAAP VVVGHARLSR VLNQPQSLLV ETVVVARALR GRGFGRRLME GLEVFARARG FRKLHLTTHD QVHFYTHLGY QLGEPVQGLV FTSRRLPATL LNAFPTAPSP RPPRKAPNLT AQAAPRGPKG PPLPPPPPLP ECLTISPPVP SGPPSKSLLE TQYQNVRGRP IFWMEKDI.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
ACYP1 HumanDescription:
Acylphosphatase 1 Human Recombinant
Acylphosphatase-1, Acylphosphatase, erythrocyte isozyme, Acylphosphatase, organ-common type isozyme, Acylphosphate phosphohydrolase 1, ACYP1, ACYPE.
Product # :
ENZ-078Price :
Quantity :
Shipping Method :
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Description
ACYP1 Human Recombinant fused with a 23 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 122 amino acids (1-99 a.a.) and having a molecular mass of 13.6kDa. The ACYP1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ACYP1 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Erythrocyte acylphosphatase (ACYP1) is a cytosolic enzyme which catalyzes the hydrolysis of the carboxyl-phosphate bond of acylphosphates. There are two acylphophatase isoenzymes: ACYP1 and ACYP2. These isoenzymes share 60% homology and have the same substrate specificity, even though ACYP1 has a higher catalytic activity than ACYP2.
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Synonyms
Acylphosphatase-1, Acylphosphatase, erythrocyte isozyme, Acylphosphatase, organ-common type isozyme, Acylphosphate phosphohydrolase 1, ACYP1, ACYPE.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAEGNTL ISVDYEIFGK VQGVFFRKHT QAEGKKLGLV GWVQNTDRGT VQGQLQGPIS KVRHMQEWLE TRGSPKSHID KANFNNEKVI LKLDYSDFQI VK.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
GLA HumanDescription:
Alpha-Galactosidase Human Recombinant
Alpha-galactosidase A, Alpha-D-galactosidase A, Alpha-D-galactoside galactohydrolase, Melibiase, GLA, GALA.
Product # :
ENZ-926Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
GLA produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 406 amino acids (32-429 a.a.) and having a molecular mass of 46.4kDa GLA is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
GLA protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Alpha-galactosidase A (GLA) is a homodimeric glycoprotein which hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins. GLA catalyzes the hydrolysis of melibiose into galactose and glucose. Various mutations in the GLA gene affect the synthesis, processing, and stability of this enzyme, which causes Fabry disease (a rare lysosomal storage disorder which results from a failure to catabolize alpha-D-galactosyl glycolipid moieties).
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Synonyms
Alpha-galactosidase A, Alpha-D-galactosidase A, Alpha-D-galactoside galactohydrolase, Melibiase, GLA, GALA.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
LDNGLARTPT MGWLHWERFM CNLDCQEEPD SCISEKLFME MAELMVSEGW KDAGYEYLCI DDCWMAPQRD SEGRLQADPQ RFPHGIRQLA NYVHSKGLKL GIYADVGNKT CAGFPGSFGY YDIDAQTFAD WGVDLLKFDG CYCDSLENLA DGYKHMSLAL NRTGRSIVYS CEWPLYMWPF QKPNYTEIRQ YCNHWRNFAD IDDSWKSIKS ILDWTSFNQE RIVDVAGPGG WNDPDMLVIG NFGLSWNQQV TQMALWAIMA APLFMSNDLR HISPQAKALL QDKDVIAINQ DPLGKQGYQL RQGDNFEVWE RPLSGLAWAV AMINRQEIGG PRSYTIAVAS LGKGVACNPA CFITQLLPVK RKLGFYEWTS RLRSHINPTG TVLLQLENTM QMSLKDLLVE HHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
PRSS7 HumanDescription:
Protease Serine 7 Human Recombinant
PRSS7,ENTK,Protease, Serine, 7 (Enterokinase), Transmembrane Protease, Serine 15, Serine Protease 7, Enteropeptidase, EC 3.4.21.9, Transmembrane Protease Serine 15,Enterokinase Catalytic Subunit, Proenterokinase, Enterokinase, EC 3.4.21.
Product # :
ENZ-850Price :
Quantity :
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Description
PRSS7 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 237 amino acids (785-1019 a.a.) and having a molecular mass of 26.4kDa. The PRSS7 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PRSS7 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
-
Introduction
Protease Serine 7, also known as PRSS7, is in charge of initiating the activation of pancreatic proteolytic proenzymes such as trypsin, chymotrypsin and carboxypeptidase A. PRSS7 catalyzes the conversion of trypsinogen to trypsin which in turn activates other proenzymes including chymotrypsinogen, procarboxypeptidases, as well as proelastases.
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Synonyms
PRSS7,ENTK,Protease, Serine, 7 (Enterokinase), Transmembrane Protease, Serine 15, Serine Protease 7, Enteropeptidase, EC 3.4.21.9, Transmembrane Protease Serine 15,Enterokinase Catalytic Subunit, Proenterokinase, Enterokinase, EC 3.4.21.
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Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MAIVGGSNAK EGAWPWVVGL YYGGRLLCGA SLVSSDWLVS AAHCVYGRNL EPSKWTAILG LHMKSNLTSP QTVPRLIDEI VINPHYNRRR KDNDIAMMHL EFKVNYTDYI QPICLPEENQ VFPPGRNCSI AGWGTVVYQG TTANILQEAD VPLLSNERCQ QQMPEYNITE NMICAGYEEG GIDSCQGDSG GPLMCQENNR WFLAGVTSFG YKCALPNRPG VYARVSRFTE WIQSFLH
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
UCHL3 HumanDescription:
Ubiquitin Carboxyl-Terminal Esterase L3 Human Recombinant
Ubiquitin Carboxyl-Terminal Esterase L3 (ubiquitin thiolesterase), UCH-L3, Ubiquitin Carboxyl-Terminal Hydrolase Isozyme L3, EC 3.4.19.12.
Product # :
ENZ-057Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
UCHL3 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 250 amino acids (1-230a.a.) and having a molecular mass of 28.3kDa.UCHL3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The UCHL3 protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0)
1mM DTT and 10% glycerol.Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
Specific activity: >3,000 pmole/min/ug. Measured by the hydrolysis of Ubiquitin-AMC at pH 8.0, at 37C.More Info
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Introduction
Ubiquitin carboxyl-terminal hydrolase isozyme L3 belongs to a gene family whose products hydrolyze small C-terminal adducts of ubiquitin to produce the ubiquitin monomer. UCHL3 takes part in the regulation of neuronal development and spermatogenesis and is associated to neurodegenerative diseases. UCHL3 has a 54% homology to UCHL1.
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Synonyms
Ubiquitin Carboxyl-Terminal Esterase L3 (ubiquitin thiolesterase), UCH-L3, Ubiquitin Carboxyl-Terminal Hydrolase Isozyme L3, EC 3.4.19.12.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MEGQRWLPLE ANPEVTNQFL KQLGLHPNWQ FVDVYGMDPE LLSMVPRPVC AVLLLFPITE KYEVFRTEEE EKIKSQGQDV TSSVYFMKQT ISNACGTIGL IHAIANNKDK MHFESGSTLK KFLEESVSMS PEERARYLEN YDAIRVTHET SAHEGQTEAP SIDEKVDLHF IALVHVDGHL YELDGRKPFP INHGETSDET LLEDAIEVCK KFMERDPDEL RFNAIALSAA
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
PRSS28 MouseDescription:
Protease Serine 28 Mouse Recombinant
Serine protease 28, Implantation serine proteinase 1, ISP-1, Strypsin, Tryptase-like proteinase.
Product # :
ENZ-987Price :
Quantity :
Shipping Method :
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Description
PRSS28 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 256 amino acids (27-274a.a.) and having a molecular mass of 28.7kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). PRSS28 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
PRSS28 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Serine protease 28, also known as Prss28, is a member of the S1 serine proteinase family with a conserved Histidine-Aspartic Acid-Serine catalytic triad. Prss28 shows mixed substrate specificity which silences signaling through proteinase-activated receptors. Furthermore, Prss28 is involved with embryo hatching and its activity is vital for successful implantation.
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Synonyms
Serine protease 28, Implantation serine proteinase 1, ISP-1, Strypsin, Tryptase-like proteinase.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
KPVGIVGGQC TPPGKWPWQV SLRMYSYEVN SWVHICGGSI IHPQWILTAA HCIQSQDADP AVYRVQVGEV YLYKEQELLN ISRIIIHPDY NDVSKRFDLA LMQLTALLVT STNVSPVSLP KDSSTFDSTD QCWLVGWGNL LQRVPLQPPY QLHEVKIPIQ DNKSCKRAYR KKSSDEHKAV AIFDDMLCAG TSGRGPCFGD SGGPLVCWKS NKWIQVGVVS KGIDCSNNLP SIFSRVQSSL AWIHQHIQLE HHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
MGLL Human, ActiveDescription:
Monoglyceride Lipase Human Recombinant, Active
Monoglyceride lipase, MGL, HU-K5, Lysophospholipase homolog, Lysophospholipase-like, Monoacylglycerol lipase, MAGL, MGLL, HUK5.
Product # :
ENZ-983Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
MGLL Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 333 amino acids (1-313 a.a.) and having a molecular mass of 36.4kDa. The MGLL is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MGLL solution (0.5mg/ml) contains 20mM Tris-HCl Buffer (pH 8.0) and 10% Glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 170 units/mg, and is defined as the amount of enzyme that hydrolyze 1.0 umole of p-nitrophenyl butyrate to pnitrophenol per minute at pH 7.5 at 25C.More Info
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Introduction
MGLL is a membrane-associated member of the serine hydrolase superfamily. MGLL is expressed in abundance in skeletal muscle and adipose tissue. MGLL functions jointly with hormone-sensitive lipase (LIPE) to hydrolyze intracellular triglyceride stores in adipocytes and other cells to fatty acids and glycerol. MGLL may also complement lipoprotein lipase (LPL) in completing hydrolysis of monoglycerides resulting from degradation of lipoprotein triglycerides.
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Synonyms
Monoglyceride lipase, MGL, HU-K5, Lysophospholipase homolog, Lysophospholipase-like, Monoacylglycerol lipase, MAGL, MGLL, HUK5.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH METGPEDPSS MPEESSPRRT PQSIPYQDLP HLVNADGQYL FCRYWKPTGT PKALIFVSHG AGEHSGRYEE LARMLMGLDL LVFAHDHVGH GQSEGERMVV SDFHVFVRDV LQHVDSMQKD YPGLPVFLLG HSMGGAIAIL TAAERPGHFA GMVLISPLVL ANPESATTFK VLAAKVLNLV LPNLSLGPID SSVLSRNKTE VDIYNSDPLI CRAGLKVCFG IQLLNAVSRV ERALPKLTVP FLLLQGSADR LCDSKGAYLL MELAKSQDKT LKIYEGAYHV LHKELPEVTN SVFHEINMWV SQRTATAGTA SPP.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
RPIA HumanDescription:
Ribose 5-Phosphate Isomerase A Human Recombinant
Ribose-5-phosphate isomerase, Phosphoriboisomerase, RPIA, RPI.
Product # :
ENZ-228Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
RPIA Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 331 amino acids (1-311) and having a molecular mass of 35.4kDa.RPIA is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The RPIA solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT,40% glycerol, 200mM NaCl, 2mM EDTA and 0.2mM PMSF.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
Ribose-5-phosphate isomerase (RPIA) is a member of the ribose 5-phosphate isomerase family. RPIA is an enzyme which catalyzes the conversion between ribose-5-phosphate (R5P) and ribulose-5-phosphate (Ru5P). RPI occurs as 2 separate proteins forms, termed RPIA and RPIB. RPIA has a vital role in the metabolism of plants and animals, as it is involved in the Calvin cycle which takes place in plants, and the pentose phosphate pathway which occurs in plants as well as animals.
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Synonyms
Ribose-5-phosphate isomerase, Phosphoriboisomerase, RPIA, RPI.
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Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MQRPGPFSTL YGRVLAPLPG RAGGAASGGG GNSWDLPGSH VRLPGRAQSG TRGGAGNTST SCGDSNSICP APSTMSKAEE AKKLAGRAAV ENHVRNNQVL GIGSGSTIVH AVQRIAERVK QENLNLVCIP TSFQARQLIL QYGLTLSDLD RHPEIDLAID GADEVDADLN LIKGGGGCLT QEKIVAGYAS RFIVIADFRK DSKNLGDQWH KGIPIEVIPM AYVPVSRAVS QKFGGVVELR MAVNKAGPVV TDNGNFILDW KFDRVHKWSE VNTAIKMIPG VVDTGLFINM AERVYFGMQD GSVNMREKPF C.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
PON1 Human (170-232)Description:
Paraoxonase-1 (170-232) Human Recombinant
Serum paraoxonase, arylesterase 1, EC 3.1.1.2, EC 3.1.8.1, PON 1.
Product # :
ENZ-1198Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The PON1 Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The PON1 His-Tagged Fusion Protein, produced in E. coli, is a 13kDa protein containing 63 amino acid residues of the PON1 Human, 170-232 amino acids.
Source
Escherichia Coli.
Formulation
Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Synonyms
Serum paraoxonase, arylesterase 1, EC 3.1.1.2, EC 3.1.8.1, PON 1.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized PON1 at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile!
Please filter the product by an appropriate sterile filter before using it on cell culture.
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Background
PON1takes part in the detoxification of organophosphate insecticides such as parathion.
PON1 is related to high-density lipoprotein (HDL) in the plasma and takes an important part in lipid metabolism and antioxidant defense.
PON1 was first known for its ability to protect against oxidative stress and hydrolyze organophosphates.
PON1 reduces oxidative stress by preventing the oxidation of lipids in LDL particles, which is extremely important in mitigating atherosclerosis and other cardiovascular diseases.
PON1 has anti-inflammatory effects which help reduce inflammatory markers in different disease states.
PON1 takes part in cholesterol metabolism, influencing the stability and formation of HDL particles, which are vital for lipid transport and reverse cholesterol efflux.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
SAT2 HumanDescription:
Spermidine/Spermine N1-Acetyltransferase 2 Human Recombinant
Spermidine/spermine N1-acetyltransferase family member 2, Polyamine N-acetyltransferase 2, SSAT2, Thialysine N-epsilon-acetyltransferase, diamine acetyltransferase 2, S, EC 2.3.1.57.
Product # :
ENZ-587Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SAT2 Human Recombinant produced in E. coli is a single polypeptide chain containing 190 amino acids (1-170) and having a molecular mass of 21.0kDa.SAT2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The SAT2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Spermidine/Spermine N1-Acetyltransferase 2, also known as SAT2 catalyzes the acetylation of polyamines (Acetyl-CoA + an alkane-alpha,omega-diamine = CoA + an N-acetyldiamine).
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Synonyms
Spermidine/spermine N1-acetyltransferase family member 2, Polyamine N-acetyltransferase 2, SSAT2, Thialysine N-epsilon-acetyltransferase, diamine acetyltransferase 2, S, EC 2.3.1.57.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MASVRIREAK EGDCGDILRL IRELAEFEKL SDQVKISEEA LRADGFGDNP FYHCLVAEIL PAPGKLLGPC VVGYGIYYFI YSTWKGRTIY LEDIYVMPEY RGQGIGSKII KKVAEVALDK GCSQFRLAVL DWNQRAMDLY KALGAQDLTE AEGWHFFCFQ GEATRKLAGK
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
ASPRV1 HumanDescription:
Aspartic Peptidase, Retroviral-Like 1 Human Recombinant
Retroviral-like aspartic protease 1, Skin-specific retroviral-like aspartic protease, SASPase, Skin aspartic protease, TPA-inducible aspartic proteinase-like protein, TAPS, ASPRV1, SASP, MUNO.
Product # :
ENZ-659Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ASPRV1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 159 amino acids (191-326) and having a molecular mass of 17.2kDa.ASPRV1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ASPRV1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Aspartic Peptidase, Retroviral-Like 1 (ASPRV1) is a protein which contains one peptidase A2 domain. ASPRV1 undergoes autocleavage which is essential for activation of the protein. ASPRV1 is expressed mostly in the granular layer of the epidermis and inner root sheath of hair follicles and localized to membrane region. In the psoriatic skin, ASPRV1 is expressed throughout the stratum corneum. In the ulcerated skin, ASPRV1 is expressed in the stratum granulosum of intact epidermis; however it is virtually nonexistent from ulcerated regions. In addition, ASPRV1 is expressed in differentiated areas of squamous cell carcinomas but not in the undifferentiated tumors.
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Synonyms
Retroviral-like aspartic protease 1, Skin-specific retroviral-like aspartic protease, SASPase, Skin aspartic protease, TPA-inducible aspartic proteinase-like protein, TAPS, ASPRV1, SASP, MUNO.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSSMGKGYY LKGKIGKVPV RFLVDSGAQV SVVHPNLWEE VTDGDLDTLQ PFENVVKVAN GAEMKILGVW DTAVSLGKLK LKAQFLVANA SAEEAIIGTD VLQDHNAILD FEHRTCTLKG KKFRLLPVGG SLEDEFDLE.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
ACOT13 HumanDescription:
Acyl-CoA Thioesterase 13 Human Recombinant
Acyl-coenzyme A thioesterase 13, Acyl-CoA thioesterase 13, Thioesterase superfamily member 2, ACOT13, THEM2, HT012, MGC4961, PNAS-27, ACOT13.
Product # :
ENZ-004Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ACOT13 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 160 amino acids (1-140 a.a.) and having a molecular mass of 17.1kDa. The ACOT13 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ACOT13 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Acyl-coenzyme A thioesterase 13 (ACOT13) belongs to the thioesterase subfamily of esterase family. ACOT13 is highly expressed in the kidney with moderate expression in the brain, liver and intestines. ACOT13 contains a hotdog-fold and is thought to co-localize with microtubules, possibly having a role in cellular proliferation events. Deletion of a segment of the q arm of chromosome 6 is linked to early onset intestinal cancer, suggesting the presence of a cancer susceptibility locus.
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Synonyms
Acyl-coenzyme A thioesterase 13, Acyl-CoA thioesterase 13, Thioesterase superfamily member 2, ACOT13, THEM2, HT012, MGC4961, PNAS-27, ACOT13.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MTSMTQSLRE VIKAMTKARN FERVLGKITL VSAAPGKVIC EMKVEEEHTN AIGTLHGGLT ATLVDNISTM ALLCTERGAP GVSVDMNITY MSPAKLGEDI VITAHVLKQG KTLAFTSVDL TNKATGKLIA QGRHTKHLGN.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.